Rang C, Lacey L A, Frutos R
CIRAD, Avenue Agropolis, B.P. 5035, 34032 Montpellier Cedex 1, France.
Curr Microbiol. 2000 Mar;40(3):200-4. doi: 10.1007/s002849910040.
Crystal proteins from Bacillus thuringiensis subsp. thompsoni strain HnC are active against the codling moth, Cydia pomonella, a major pest of orchards. Inclusion bodies purified from strain HnC displayed an LC(50) of 3.34 x 10(-3) microgram/microliter. HnC-purified crystals were tenfold more active than Cry2Aa and Cry1Aa toxins, and 100-fold more toxic than Cry1Ab. The 34-kDa and 40-kDa proteins contained in HnC inclusion bodies were shown to act synergistically. The toxicity of crystal proteins produced by the recombinant B. thuringiensis strain BT-OP expressing the full-length native operon was about tenfold higher than that of the 34-kDa protein. When the gene encoding the non-insecticidal 40-kDa protein, which is not active, was introduced into the recombinant strain producing only the 34-kDa protein, the toxicity was raised tenfold and was similar to that of the strain BT-OP.
苏云金芽孢杆菌汤普森亚种HnC菌株的晶体蛋白对果园主要害虫苹果蠹蛾（Cydia pomonella）具有活性。从HnC菌株纯化的包涵体显示出的半数致死浓度（LC50）为3.34×10⁻³微克/微升。HnC纯化晶体的活性比Cry2Aa和Cry1Aa毒素高10倍，毒性比Cry1Ab高100倍。HnC包涵体中含有的34 kDa和40 kDa蛋白显示出协同作用。表达全长天然操纵子的重组苏云金芽孢杆菌菌株BT-OP产生的晶体蛋白毒性比34 kDa蛋白高约10倍。当将编码无活性的非杀虫性40 kDa蛋白的基因导入仅产生34 kDa蛋白的重组菌株中时，毒性提高了10倍，与菌株BT-OP的毒性相似。
